SCIENTIFIC ABSTRACT OREKHOVICH, V.N. - OREL, N.D.

• Document Type: CREST
• Collection: Scientific Abstracts
• Document Number (FOIA) /ESDN (CREST): CIA-RDP86-00513R001238130004-9
• Release Decision: RIF
• Original Classification: S
• Document Page Count: 100
• Document Creation Date: January 3, 2017
• Document Release Date: August 1, 2000
• Sequence Number: 4
• Publication Date: December 31, 1967
• Content Type: SCIENTIFIC ABSTRACT

INNANT, M.I.; I3VCHUX. T.P.; OHEKHOVICH. V.N.
Mechanism of the incorporation of libeled amino acids into nroteins.
Biokhimiia 24 no.2:177-180 Mr-Ap 159. (MIRA 12:7)
1. Institute of Biological and Medical Chemistry, Aondemy of Redical
Sciences of the U.S.S.R., Moscow.
(MHIONINS, metabolism,
serum albumin incorporationt radiotracer studies (Hus))
(SILHUH AUUMIN,
toethioulne incorporation. radiotracer studies Ohis))

ORFXHOVICH. V.N.; KHOIDTIOVA, O.S.; CIUMINDV. M.P.
Vixation of proteinsees by wool. Biokhtmiia 24 uo~2:353-356 Mr-Ap '59
(MIRA 12:7)
1. Institute of Biolopical and Medical Chemistry, Academy of Medical
Sciences of the U.S.S.R., Moscow.
(PIROTUSH
binding by animal hair (Rua))
(HAIR,
binding of protea9ee by animal hair (Rua))

ORZKHOVICH. V.11.; SHCHUX11LIk, L.A.; TSI CHZKMI-U [Ch'i Chang-wuj ; SPIRICHEV, V.B.
Role of the natiire of amino acid and acyl radicals in enzynati~
synthesis of I-acyl-amino acids by acylase I. Biokhimiia 24
no.4:667-671 JI-J~g '59- (MIRA 12:11)
1. Institut biologicheskoy I meditainskoy Ir-himii Akademil
mectitainakikh nauk SSSR, Moskva.
(ESTARASES chem. )
(AIII110 ACIDS chem.)
Vo

17(3)
~UTHO-IS. 1,1,azurov, V. I., Ore~-ho,~ich, V. N.,
Me mb e r, _77-37~
TITLE: Inclusion of the !Zad~oactive Glycine B Into the u- and ~'-Com-
ponents of i-rocollagene (Vklyucheniye radioaktivno..-o ~,litsina v
i 0-kom2onenty prokollageiia)
PEPIODIC'.L: Dokl-.dy Aa6eniii nauk 1959, Vol 125, Nr 2, pp 40,81-410
t'~B.)' T'. i AT -h,? mcloculo in ~he qkin of rfttB cl-composes with
the action, -if urea, ilc,1113, ~-inl heatin,; into two 1~rotein com-
ponents (~ef 1). The latter represeni tro -Iaximl i.r t~li, -altra-
centrifii-e. Thu 1i ,-liter comporient ((.) has a mclecul-ir .-,ei -ht
of 125,u0l,~ the lic'-.vier one (P) has a inoloculnr woicht of
295,000, L;inco the v4ei,,7ht ratio a in the T,rocolla~:-ene
molecule- w-;s 1 : 1, it wis assumed that this moleculo c-)nsists
of two u ~~z~rticl*-3 and one p particle (Ref 2). 1,1ean-r.ille, the
com,-onerts hnve been 4riventilrated rather z-11 from
9 point ci~ view. Yet it cannot LC: -)~i~nt '11 - 12 1
absolutely ~iccor'.in,,, to these data that the native i,i,,)collagene
mol,,cule r(,1;r-:,t,,!its -i crimpliox of two structurnl ontiti,r.
Card 1/3 The-efore the problem -entioned in the title yvif3 int-restin.,

Inclusion of the Radioactive Glycine B Into the Sr,'V120- 12 rl-~ -4.:--/'64
a- and P-Components of :-rocollagene
with respect to the rate of influence of both components.
White rats were intraperitoneally injected with C14 glycine
marked on carboxyl. The animals were killed 3, 6, 1", 18, 24,
48, and 144 hours after the injection. It was proved that the
inclusion intensity of C14 into the a-component is about
three times as strong as in the case of the P-component
(Fig 1). The arithmetic mean value of the radioactivity of
both components was about equal to the activity of the whole
preparation a + P. Apparenzly, this confirms also the above-
mentioned weij~ht ratio of 1 : 1 of the components. Figiire 1
further indicates that the inclusion intensity of' C14 attains
a rather high level 3 hours after the injection. The highest
degree of radioactivity is attained after 48 hours. In the
u-component it was attained aftei- 18 hours and in the
P-component after 48 hours. In the course of the experiment
this intensity of the a-component was 3 to 4 times as high
as that of the P-component, The authors are not able to
Card 2/3 explain this difference. They suppose that there is an

Inclusion of the Radioactive Slycine B Into the SOV/20-12r)-2-48/64
a- and P-Components of Procollagene
independent synthesis of both components within the cell. The
results obtained are insufficient for drawing definite con-
clusions on the nature of these components. They indicate,
however, that certain sections of the polypeptide chain of
the procollagene molecule are not equivalent as far as their
bioloCical properties are concerned. There are 1 fi(Ture and
6 referencec, 5 of which are Soviet.
ASSOCIATION: Institut bdo'ogicheskoy ; meditsinakoy khimii Akademii medit-
sinskikh nauk SSSR (Institute of Biolo,-,ical and Medical
Chemistry of the Academy of 11.1edical Sciences, USSR)
SUBMITTED: December 9, 19~8
Card 3/3

PANTIYNV. V.A.; ORBIROVICH, V.I.
Graphs for the calculation of the ion strength of the most
utilized buffer solutions. Lab.dolo 6 no.2:11-17 W-Ap ~60.
(MIRA 13:6)
1. Institut biologichemkoy i meditsinskoy kh1mii (dir. - prof.
V.N. Orekhovich), Moskva.
(IONO
4-r

OREKHOVICH, V.N.
"Biophysical science; e study program". Reviewed by V.N.Orekhovich.
Vop.med.khim. 6 no, j442 JI-Ag 160. (MIRA 140)
tBIOPHYSICS)

--ORF-KH(YVICH, V-,N.,-, PLOTNIKOVA, N.Ye.
Specific activity of glycerin on the blood vessel valls. V4p.
med.1rhim. 6 no.5:544 S-0 160, (HIM 14-1)
1. Institut biologicheskoy i meditsinskoy 1rhimij AMN SSSR.
(GLYCEROL) (BLOOD VMSILS)

KLZUROV, V.I.; ORMOVICH, V.N.
Sti4ying the c